Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12.
J Biol Chem
; 285(44): 33992-4003, 2010 Oct 29.
Article
em En
| MEDLINE
| ID: mdl-20739285
ABSTRACT
Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19 S regulatory particle where it binds to subunits of both the base and lid subparticles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the von Willebrand factor type A domain and characterizing the full-length protein by NMR. We demonstrate that the single Ub-interacting motif (UIM) of SpRpn10 forms a 11 complex with Lys(48)-linked diUb, which it binds selectively over monoUb and Lys(63)-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys(48)-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Schizosaccharomyces
/
Proteínas de Transporte
/
Proteínas de Schizosaccharomyces pombe
/
Poliubiquitina
/
Complexo de Endopeptidases do Proteassoma
Limite:
Humans
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article